The ESCRT-III-Interacting Deubiquitinating Enzyme AMSH3 is Essential for Degradation of Ubiquitinated Membrane Proteins in Arabidopsis thaliana

Lade...
Vorschaubild
Dateien
Katsiarimpa_0-398719.pdf
Katsiarimpa_0-398719.pdfGröße: 448.55 KBDownloads: 225
Datum
2014
Autor:innen
Katsiarimpa, Anthi
Munoz, Alfonso
Kalinowska, Kamila
Uemura, Tomohiro
Rojo, Enrique
Herausgeber:innen
Kontakt
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
DOI (zitierfähiger Link)
ArXiv-ID
Internationale Patentnummer
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Open Access Green
Sammlungen
Core Facility der Universität Konstanz
Gesperrt bis
Titel in einer weiteren Sprache
Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published
Erschienen in
Plant and Cell Physiology. 2014, 55(4), pp. 727-736. ISSN 0032-0781. eISSN 1471-9053. Available under: doi: 10.1093/pcp/pcu019
Zusammenfassung

Post-translational modification by ubiquitin plays a key role in the regulation of endocytic degradation in which ubiquitinated plasma membrane cargos are transported to the vacuole for degradation dependent on the ESCRT (endosomal sorting complex required for transport) machinery. Arabidopsis AMSH3 (ASSOCIATED MOLECULE WITH THE SH3 DOMAIN OF STAM 3) is a deubiquitinating enzyme that interacts with at least two subunits of the ESCRT-III machinery, VPS2.1 and VPS24.1. amsh3 null mutation causes seedling lethality, and amsh3 null mutants show defects in multiple intracellular trafficking pathways. In this study, we further analyzed the amsh3 mutant phenotype and showed that amsh3 accumulates membrane-associated ubiquitinated proteins, supporting the indication that AMSH3 functions in ubiquitin-mediated endocytic degradation. In accordance with this, an enzymatic inactive variant of AMSH3 inhibits the AvrPtoB-dependent endocytic degradation of CERK1 (CHITIN ELICITOR RECEPTOR KINASE 1). Furthermore, we showed that the interaction of AMSH3 with ESCRT-III is important for its function in planta. Together, our data indicate the importance of AMSH3 and the AMSH3-ESCRT-III interaction for deubiquitination and degradation of ubiquitinated membrane substrates in plants.

Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
570 Biowissenschaften, Biologie
Schlagwörter
AMSH ; Arabidopsis thaliana ; ESCRT ; Ubiquitin
Konferenz
Rezension
undefined / . - undefined, undefined
Forschungsvorhaben
Organisationseinheiten
Zeitschriftenheft
Datensätze
Zitieren
ISO 690KATSIARIMPA, Anthi, Alfonso MUNOZ, Kamila KALINOWSKA, Tomohiro UEMURA, Enrique ROJO, Erika ISONO, 2014. The ESCRT-III-Interacting Deubiquitinating Enzyme AMSH3 is Essential for Degradation of Ubiquitinated Membrane Proteins in Arabidopsis thaliana. In: Plant and Cell Physiology. 2014, 55(4), pp. 727-736. ISSN 0032-0781. eISSN 1471-9053. Available under: doi: 10.1093/pcp/pcu019
BibTex
@article{Katsiarimpa2014-04-10ESCRT-38158,
  year={2014},
  doi={10.1093/pcp/pcu019},
  title={The ESCRT-III-Interacting Deubiquitinating Enzyme AMSH3 is Essential for Degradation of Ubiquitinated Membrane Proteins in Arabidopsis thaliana},
  number={4},
  volume={55},
  issn={0032-0781},
  journal={Plant and Cell Physiology},
  pages={727--736},
  author={Katsiarimpa, Anthi and Munoz, Alfonso and Kalinowska, Kamila and Uemura, Tomohiro and Rojo, Enrique and Isono, Erika}
}
RDF
<rdf:RDF
    xmlns:dcterms="http://purl.org/dc/terms/"
    xmlns:dc="http://purl.org/dc/elements/1.1/"
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:bibo="http://purl.org/ontology/bibo/"
    xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
    xmlns:foaf="http://xmlns.com/foaf/0.1/"
    xmlns:void="http://rdfs.org/ns/void#"
    xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > 
  <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/38158">
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/38158"/>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:contributor>Rojo, Enrique</dc:contributor>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-03-27T14:32:49Z</dc:date>
    <dc:creator>Rojo, Enrique</dc:creator>
    <dc:creator>Uemura, Tomohiro</dc:creator>
    <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
    <dc:creator>Katsiarimpa, Anthi</dc:creator>
    <dc:contributor>Isono, Erika</dc:contributor>
    <dc:creator>Munoz, Alfonso</dc:creator>
    <dcterms:title>The ESCRT-III-Interacting Deubiquitinating Enzyme AMSH3 is Essential for Degradation of Ubiquitinated Membrane Proteins in Arabidopsis thaliana</dcterms:title>
    <dc:creator>Isono, Erika</dc:creator>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/38158/3/Katsiarimpa_0-398719.pdf"/>
    <dc:contributor>Uemura, Tomohiro</dc:contributor>
    <dc:contributor>Munoz, Alfonso</dc:contributor>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-03-27T14:32:49Z</dcterms:available>
    <dcterms:issued>2014-04-10</dcterms:issued>
    <dcterms:abstract xml:lang="eng">Post-translational modification by ubiquitin plays a key role in the regulation of endocytic degradation in which ubiquitinated plasma membrane cargos are transported to the vacuole for degradation dependent on the ESCRT (endosomal sorting complex required for transport) machinery. Arabidopsis AMSH3 (ASSOCIATED MOLECULE WITH THE SH3 DOMAIN OF STAM 3) is a deubiquitinating enzyme that interacts with at least two subunits of the ESCRT-III machinery, VPS2.1 and VPS24.1. amsh3 null mutation causes seedling lethality, and amsh3 null mutants show defects in multiple intracellular trafficking pathways. In this study, we further analyzed the amsh3 mutant phenotype and showed that amsh3 accumulates membrane-associated ubiquitinated proteins, supporting the indication that AMSH3 functions in ubiquitin-mediated endocytic degradation. In accordance with this, an enzymatic inactive variant of AMSH3 inhibits the AvrPtoB-dependent endocytic degradation of CERK1 (CHITIN ELICITOR RECEPTOR KINASE 1). Furthermore, we showed that the interaction of AMSH3 with ESCRT-III is important for its function in planta. Together, our data indicate the importance of AMSH3 and the AMSH3-ESCRT-III interaction for deubiquitination and degradation of ubiquitinated membrane substrates in plants.</dcterms:abstract>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:creator>Kalinowska, Kamila</dc:creator>
    <dc:contributor>Katsiarimpa, Anthi</dc:contributor>
    <dc:language>eng</dc:language>
    <dc:rights>terms-of-use</dc:rights>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/38158/3/Katsiarimpa_0-398719.pdf"/>
    <dc:contributor>Kalinowska, Kamila</dc:contributor>
  </rdf:Description>
</rdf:RDF>
Interner Vermerk
xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter
Kontakt
URL der Originalveröffentl.
Prüfdatum der URL
Prüfungsdatum der Dissertation
Finanzierungsart
Kommentar zur Publikation
Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Nein
Begutachtet
Diese Publikation teilen